The leukotrienes are a group of proinflammatory lipid mediators that have been implicated in the pathogenesis and progression of atherosclerosis. LTA4H, or leukotriene A4 hydrolase, is a bifunctional enzyme with aminopeptidase and epoxide hydrolase activities that utilize a single zinc active site (1). The aminopeptidase activity of LTA4H, but not epoxide hydrolase activity, highly depends on certain monovalent anions, especially chloride and thiocyanate ions (2). As a member of the peptidase M1 family, LTA4H hydrolyzes an epoxide moiety of leukotriene A4 (LTA-4) to form leukotriene B4 (LTB-4), which acts as a chemoattractant and an activator of inflammatory responses mediated by binding to G-protein-coupled receptors BLT1 and BLT2 (1, 3).
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